+Open data
-Basic information
Entry | Database: PDB / ID: 7bxw | |||||||||
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Title | Crystal structure ofF RTT109 FROM Candida albicans | |||||||||
Components | Histone acetyltransferase RTT109 | |||||||||
Keywords | TRANSFERASE / HISTONE / ACETYLATION / DNA REPLICATION / NUCLEOSOME ASSEMBLY / DNA DAMAGE | |||||||||
Function / homology | Function and homology information regulation of phenotypic switching / negative regulation of filamentous growth of a population of unicellular organisms / filamentous growth of a population of unicellular organisms / histone H3K56 acetyltransferase activity / phenotypic switching / DNA replication-dependent chromatin disassembly / filamentous growth / histone H3 acetyltransferase activity / histone acetyltransferase / DNA damage response ...regulation of phenotypic switching / negative regulation of filamentous growth of a population of unicellular organisms / filamentous growth of a population of unicellular organisms / histone H3K56 acetyltransferase activity / phenotypic switching / DNA replication-dependent chromatin disassembly / filamentous growth / histone H3 acetyltransferase activity / histone acetyltransferase / DNA damage response / regulation of DNA-templated transcription / nucleus Similarity search - Function | |||||||||
Biological species | Candida albicans (yeast) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.77629297561 Å | |||||||||
Authors | Lei, J.H. / Chen, Y.P. / Lu, D.R. / Su, D. | |||||||||
Funding support | China, 1items
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Citation | Journal: To be published Title: Crystal structure ofF RTT109 FROM Candida albicans Authors: Su, D. / Hu, Q. #1: Journal: J. Biol. Chem / Year: 2011 Title: Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex Authors: Su, D. / Hu, Q. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7bxw.cif.gz | 177.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7bxw.ent.gz | 114.2 KB | Display | PDB format |
PDBx/mmJSON format | 7bxw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7bxw_validation.pdf.gz | 449.6 KB | Display | wwPDB validaton report |
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Full document | 7bxw_full_validation.pdf.gz | 452.2 KB | Display | |
Data in XML | 7bxw_validation.xml.gz | 16.7 KB | Display | |
Data in CIF | 7bxw_validation.cif.gz | 24.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bx/7bxw ftp://data.pdbj.org/pub/pdb/validation_reports/bx/7bxw | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 42028.785 Da / Num. of mol.: 1 / Mutation: S321L,S336L,S339L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Candida albicans (strain SC5314 / ATCC MYA-2876) (yeast) Strain: SC5314 / ATCC MYA-2876 / Gene: RTT109, CAALFM_CR00410WA, CaO19.7491 / Plasmid: pET-Duet1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q5AAJ8, histone acetyltransferase | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 42.3 % |
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Crystal grow | Temperature: 289.15 K / Method: vapor diffusion, hanging drop / pH: 6 / Details: 0.1 M Bis-Tris pH 6.0, 15-20% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 80 K / Ambient temp details: 77 / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.975 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 5, 2015 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.975 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.77→50 Å / Num. obs: 33152 / % possible obs: 98.4 % / Redundancy: 7.6 % / Biso Wilson estimate: 22.0078106624 Å2 / Rmerge(I) obs: 0.078 / Rpim(I) all: 0.03 / Rrim(I) all: 0.084 / Χ2: 0.802 / Net I/σ(I): 5.9 / Num. measured all: 252953 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.77629297561→49.5934705553 Å / SU ML: 0.150737498595 / Cross valid method: THROUGHOUT / σ(F): 1.38249054184 / Phase error: 20.9278720425
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.5105658116 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.77629297561→49.5934705553 Å
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Refine LS restraints |
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LS refinement shell |
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